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Database: UniProt
Entry: A0A0E0E0Z8_9ORYZ
LinkDB: A0A0E0E0Z8_9ORYZ
Original site: A0A0E0E0Z8_9ORYZ 
ID   A0A0E0E0Z8_9ORYZ        Unreviewed;       436 AA.
AC   A0A0E0E0Z8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=S-acyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
DE   AltName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI06G13790.2};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI06G13790.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI06G13790.2};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI06G13790.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC         hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC         EC=2.3.1.225; Evidence={ECO:0000256|RuleBase:RU079119};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000256|RuleBase:RU079119}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00008574, ECO:0000256|RuleBase:RU079119}.
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DR   AlphaFoldDB; A0A0E0E0Z8; -.
DR   STRING; 40149.A0A0E0E0Z8; -.
DR   EnsemblPlants; OMERI06G13790.1; OMERI06G13790.1; OMERI06G13790.
DR   EnsemblPlants; OMERI06G13790.2; OMERI06G13790.2; OMERI06G13790.
DR   Gramene; OMERI06G13790.1; OMERI06G13790.1; OMERI06G13790.
DR   Gramene; OMERI06G13790.2; OMERI06G13790.2; OMERI06G13790.
DR   eggNOG; KOG1311; Eukaryota.
DR   Proteomes; UP000008021; Chromosome 6.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   PANTHER; PTHR22883:SF317; S-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU079119}; Membrane {ECO:0000256|RuleBase:RU079119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        47..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        78..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        195..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        238..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          149..275
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          107..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  49590 MW;  8227EC6639A28454 CRC64;
     MYVPQPSRSD AAARDAGDQP RVYQVWRGSN EFFLRGRFIF GPDVRSIFLT MFLIVAPVVA
     FCVFVARHLI DDFPGDWGIS VMVVVVVFTV YDLTLLLLTS GRDPGIIPRN THPPEPEGFD
     GSNDSGVQTP QQLRLPRTKD VIVNGISVRI KYCDTCMLYR PPRCSHCSIC NNCVERFDHH
     CPWVGQCIGL RNYRFFYMFV FSTTLLCLYV FAFCWVYIIK IRNAESLSVW KAMLKTPASI
     VLIIYCFLCV WFVGGLSVFH CYLMSTNQTT YENFRYRYDR RANPYNRGVL SNFLEIFCSR
     IPPSKNNFRA RVTVEQGLQQ TRVASRGFMS PNMGKPVGDF EMGRKPVPWD EPRTAADIRD
     LEAGLGGFLD EKEGRLTHAS PDLSRDDLPA DLMEGRAGTH SRRSSWVNRT GTSESVDSMN
     AQIIAAWEAI QSDPVH
//
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